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- PDB-1r0b: Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Cr... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1r0b | ||||||
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Title | Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R State Bound to PALA, or to Product Analogues Phosphate and Citrate | ||||||
![]() | (Aspartate carbamoyltransferase ...![]() | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Huang, J. / Lipscomb, W.N. | ||||||
![]() | ![]() Title: Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R-State Bound to PALA, or to Product Analogues Citrate and Phosphate Authors: Huang, J. / Lipscomb, W.N. #1: ![]() Title: Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate ...Title: Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1A Authors: Jin, L. / Stec, B. / Lipscomb, W.N. / Kantrowitz, E.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 558 KB | Display | ![]() |
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PDB format | ![]() | 455.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1q95SC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Aspartate carbamoyltransferase ... , 2 types, 12 molecules ABCDEFGHIJKL
#1: Protein | Mass: 34337.105 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: PYRB OR B4245 OR C5345 OR Z5856 OR ECS5222 OR SF4245 OR S4507 Plasmid: pEK54 / Production host: ![]() ![]() ![]() ![]() #2: Protein | Mass: 17143.625 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Non-polymers , 4 types, 906 molecules ![](data/chem/img/FLC.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-FLC / ![]() #4: Chemical | ChemComp-PO4 / ![]() #5: Chemical | ChemComp-ZN / #6: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.96 Å3/Da / Density % sol: 58.42 % |
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Crystal grow![]() | Temperature: 294 K / Method: microdialysis / pH: 5.8 Details: sodium citrate, sodium phosphate, N-ethylmorpholine, pH 5.8, MICRODIALYSIS, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: May 12, 2002 / Details: mirrors |
Radiation | Monochromator: Horizontally bent si(111), assymetrically cut with water coooled Cu block Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.9→50 Å / Num. all: 81814 / Num. obs: 61088 / % possible obs: 74.7 % / Observed criterion σ(I): -0.9 / Redundancy: 3 % / Biso Wilson estimate: 57.6 Å2 / Rsym value: 0.077 / Net I/σ(I): 13.3 |
Reflection shell | Resolution: 2.9→3 Å / Redundancy: 2 % / Mean I/σ(I) obs: 1.8 / Num. unique all: 5461 / Rsym value: 0.46 / % possible all: 75.6 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1Q95 Resolution: 2.9→50 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 63.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.9→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.9→3 Å
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